4.5.4 · D1Biomolecules

Foundations — Enzymes — lock-and-key vs induced fit; Michaelis-Menten kinetics

1,811 words8 min readBack to topic

This page assumes nothing. If the parent note wrote a symbol, we build it here from the ground up — plain words first, then a picture, then why the topic can't live without it.


1. The players (things you can point at)


2. Concentration — the meaning of the square brackets


3. Rate — what "how fast" actually means


4. Rate constants — the little 's and their arrows


5. The two combined constants the parent builds


6. The maths tools the derivation quietly uses

Recall Straight-line template

::: is the slope (steepness), is the y-intercept (where the line crosses the vertical axis at ). The reciprocal plot fits this template exactly.


7. How the foundations feed the topic

Proteins build the enzyme

Enzyme E and its active site

Catalysis speeds without being used up

Lock-and-key vs induced fit

Enzyme-substrate complex ES

Concentration bracket notation

Rate v depends on how crowded

Chemical Kinetics rate constants k

Mechanism arrows k1 k-1 k2

Derivative equals zero steady state

Michaelis-Menten equation

Km and Vmax

Reciprocal one over x

Lineweaver-Burk straight line


Equipment checklist

Test yourself — each should feel obvious before you tackle the parent page.

What does mean, in plain words?
The concentration of substrate — how crowded the substrate is in a fixed volume.
Convert into .
.
Difference between and ?
is free (empty) enzyme right now; is total enzyme (free + bound as ES).
What is and why measure it at the start?
The initial reaction rate; measured early so the reverse reaction and product build-up don't interfere.
What does each of , , describe?
= E+S forming ES; = ES breaking back to E+S; = ES going forward to E+P.
What does mean in words?
The amount of ES is holding steady — it's formed as fast as it disappears (steady state).
In , why is there a ?
It converts the proportionality (rate ) into an equation by supplying the fixed multiple.
Small means the enzyme has…
High affinity — it reaches half its top speed at low substrate concentration.
Why does the reciprocal plot use and ?
Flipping both turns the curved hyperbola into a straight line, so slope and intercepts read off and cleanly.